Sammenlign metoder

	Kryo-EM Rekonstruktion	Homologymodellering	PPI-netværkstopologi
Fagområde	Bioinformatik	Bioinformatik	Bioinformatik
Familie	Process / pipeline	Process / pipeline	Process / pipeline
Oprindelsesår	1975	1993	2000
Ophavsperson	Joachim Frank	Andrej Sali	Peter Uetz
Type	Image reconstruction pipeline	Comparative structure prediction pipeline	Network analysis pipeline
Oprindelig kilde	Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319.	Sali, A. & Blundell, T. L. (1993). Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology, 234(3), 779-815.	Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., ... & Lomax, J. (2000). A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature, 403(6770), 623-627.
Aliasser	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	comparative modeling, template-based modeling	protein interaction networks, interactome analysis, network topology
Relaterede	3	4	3
Resumé	Cryo-electron microscopy (cryo-EM) determines three-dimensional macromolecular structures at atomic or near-atomic resolution by imaging proteins frozen in vitreous ice. Pioneered by Frank, Henderson, and others, this technique has revolutionized structural biology by enabling visualization of large, non-crystallizable complexes and capturing functional conformational states.	Homology modeling, also called comparative modeling, predicts the three-dimensional structure of a protein using an experimentally-solved structure of a homologous protein as a template. Introduced by Sali and Blundell in 1993, this method exploits the principle that homologous proteins share similar spatial structures despite differing in amino acid sequence.	Protein-protein interaction network analysis identifies and characterizes the structural properties of cellular interaction networks. Pioneered by Uetz and colleagues through large-scale yeast two-hybrid screening, this approach reveals topological features like hubs, modules, and motifs that encode functional organization and disease associations.